frdC

Summary

Gene Symbol: frdC
Description: fumarate reductase (anaerobic), membrane anchor subunit
Alias: ECK4148, JW4113
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Tseng C, Hansen A, Cotter P, Gunsalus R. Effect of cell growth rate on expression of the anaerobic respiratory pathway operons frdABCD, dmsABC, and narGHJI of Escherichia coli. J Bacteriol. 1994;176:6599-605 pubmed
    ..The cell appears to have many ways to adjust cell respiration in response to changes in cell growth conditions. ..
  2. Brandsch R, Bichler V. Covalent cofactor binding to flavoenzymes requires specific effectors. Eur J Biochem. 1989;182:125-8 pubmed
    ..Our results suggest that covalent modification and thus activation of these enzymes is dependent on specific metabolic intermediates which may act as allosteric effectors in the reaction. ..
  3. Ackrell B. Progress in understanding structure-function relationships in respiratory chain complex II. FEBS Lett. 2000;466:1-5 pubmed
    ..These offer new insights into structure-function relationships of this class of flavoenzymes, including evidence favoring protein movement during catalysis...
  4. Grundstrom T, Jaurin B, Edlund T, Normark S. Physical mapping and expression of hybrid plasmids carrying chromosomal beta-lactamase genes of Escherichia coli K-12. J Bacteriol. 1980;143:1127-34 pubmed
    ..Two second-step regulatory mutations mapped within the same 370-base pair region as ampA1. This piece of deoxyribonucleic acid therefore contains ampA, a control sequence region for ampC. ..
  5. Lemire B, Robinson J, Weiner J. Identification of membrane anchor polypeptides of Escherichia coli fumarate reductase. J Bacteriol. 1982;152:1126-31 pubmed
    ..Unlike the well-characterized two-subunit form, the holoenzyme is not dependent on anions for activity and is not labile at alkaline pH. In these respects, it more closely resembles the membrane-bound activity. ..
  6. Cole S, Guest J. Production of a soluble form of fumarate reductase by multiple gene duplication in Escherichia coli K12. Eur J Biochem. 1979;102:65-71 pubmed
    ..Production of the soluble form occurred when the binding capacity of the membrane was saturated. Both forms of fumarate reductase were enzymically active but the soluble form was readily inactivated under assay conditions. ..
  7. Westenberg D, Gunsalus R, Ackrell B, Sices H, Cecchini G. Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones. J Biol Chem. 1993;268:815-22 pubmed
    ..The hydrophobic FrdC and FrdD subunits anchor the FrdA and FrdB catalytic subunits to the inner surface of the cytoplasmic membrane and ..
  8. Rothery R, Seime A, Spiers A, Maklashina E, Schröder I, Gunsalus R, et al. Defining the Q-site of Escherichia coli fumarate reductase by site-directed mutagenesis, fluorescence quench titrations and EPR spectroscopy. FEBS J. 2005;272:313-26 pubmed
    ..titrations, EPR spectroscopy and steady-state kinetics to study the effects of site-directed mutants of FrdB, FrdC and FrdD on the proximal menaquinol (MQH(2)) binding site (Q(P)) of Escherichia coli fumarate reductase (FrdABCD) ..
  9. Hirsch C, Rasminsky M, Davis B, Lin E. A FUMARATE REDUCTASE IN ESCHERICHIA COLI DISTINCT FROM SUCCINATE DEHYDROGENASE. J Biol Chem. 1963;238:3770-4 pubmed

More Information

Publications35

  1. Condon C, Weiner J. Fumarate reductase of Escherichia coli: an investigation of function and assembly using in vivo complementation. Mol Microbiol. 1988;2:43-52 pubmed
    ..Thus separation of the DNA coding for the FRD C and FRD D proteins affected the ability of fumarate reductase to assemble into a functional complex. ..
  2. Cecchini G, Sices H, Schröder I, Gunsalus R. Aerobic inactivation of fumarate reductase from Escherichia coli by mutation of the [3Fe-4S]-quinone binding domain. J Bacteriol. 1995;177:4587-92 pubmed
    ..These data suggest that the [3Fe-4S] cluster is intimately associated with one of the quinone binding sites found n fumarate reductase and succinate dehydrogenase. ..
  3. Iverson T, Luna Chavez C, Schröder I, Cecchini G, Rees D. Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex. Curr Opin Struct Biol. 2000;10:448-55 pubmed
    ..These structures revealed the cofactor organization linking the fumarate and quinol sites, and showed a cofactor arrangement across the membrane that is suggestive of a possible energy coupling function. ..
  4. Tseng C, Albrecht J, Gunsalus R. Effect of microaerophilic cell growth conditions on expression of the aerobic (cyoABCDE and cydAB) and anaerobic (narGHJI, frdABCD, and dmsABC) respiratory pathway genes in Escherichia coli. J Bacteriol. 1996;178:1094-8 pubmed
    ..These two transcriptional regulators coordinate the hierarchial control of respiratory pathway gene expression in E. coli to ensure the optimal use of oxygen in the cell environment. ..
  5. Hagerhall C. Succinate: quinone oxidoreductases. Variations on a conserved theme. Biochim Biophys Acta. 1997;1320:107-41 pubmed
  6. Luna Chavez C, Iverson T, Rees D, Cecchini G. Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli. Protein Expr Purif. 2000;19:188-96 pubmed
    ..6 A, b = 138.1 A, and c = 275.3 A. The purification and crystallization procedures are highly reproducible and the general procedure may prove useful for Complex IIs from other sources. ..
  7. Maklashina E, Cecchini G. Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli. Arch Biochem Biophys. 1999;369:223-32 pubmed
    ..The pH activity profiles for E. coli QFR and SQR are similar showing maximal activity between pH 7.4 and 7.8, suggesting the importance of similar catalytic groups in quinol deprotonation and oxidation. ..
  8. Hagerhall C, Magnitsky S, Sled V, Schröder I, Gunsalus R, Cecchini G, et al. An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site. J Biol Chem. 1999;274:26157-64 pubmed
    ..In this work, we describe an EPR-detectable QFR semiquinone using Escherichia coli mutant QFR (FrdC E29L) and the wild-type enzyme. The SQ exhibits a g = 2...
  9. Grundstrom T, Jaurin B. Overlap between ampC and frd operons on the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1982;79:1111-5 pubmed
    ..C insertion in the promoter gave both increased transcription of ampC and a frameshift in this overlapping gene, resulting in readthrough proteins. Thus, we describe a type of very compact genetic organization of operons in prokaryotes. ..
  10. Cecchini G, Schröder I, Gunsalus R, Maklashina E. Succinate dehydrogenase and fumarate reductase from Escherichia coli. Biochim Biophys Acta. 2002;1553:140-57 pubmed
    ..The structure and function of SQR and QFR are briefly summarized in this communication and the similarities and differences in the membrane domain of the two enzymes are discussed. ..
  11. Iverson T, Luna Chavez C, Croal L, Cecchini G, Rees D. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J Biol Chem. 2002;277:16124-30 pubmed publisher
    ..This acidic residue, Glu-C29, in the E. coli enzyme may act as a proton shuttle from the quinol during enzyme turnover...
  12. Maklashina E, Hellwig P, Rothery R, Kotlyar V, Sher Y, Weiner J, et al. Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli. J Biol Chem. 2006;281:26655-64 pubmed
    ..These findings represent an example of how enzymes that are designed to accommodate either UQ or MQ at a single Q binding site may nevertheless develop sufficient plasticity at the binding pocket to react differently with MQ and UQ. ..
  13. Sucheta A, Cammack R, Weiner J, Armstrong F. Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport. Biochemistry. 1993;32:5455-65 pubmed
    ..This small boost to the catalytic current indicates that the low-potential [4Fe-4S] cluster can function as a second center for relaying electrons to the FAD. ..
  14. Cohen Ben Lulu G, Francis N, Shimoni E, Noy D, Davidov Y, Prasad K, et al. The bacterial flagellar switch complex is getting more complex. EMBO J. 2008;27:1134-44 pubmed publisher
  15. Mewies M, McIntire W, Scrutton N. Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs. Protein Sci. 1998;7:7-20 pubmed
    ..Case studies are presented for a variety of covalent flavoenzymes, from which general findings are beginning to emerge. ..
  16. Wood D, Darlison M, Wilde R, Guest J. Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Biochem J. 1984;222:519-34 pubmed
    ..These proteins resemble in size and composition, but not sequence, the membrane anchor proteins of fumarate reductase (the frdC and frdD gene products).
  17. Cole S, Condon C, Lemire B, Weiner J. Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli. Biochim Biophys Acta. 1985;811:381-403 pubmed
  18. Weiner J, Cammack R, Cole S, Condon C, Honore N, Lemire B, et al. A mutant of Escherichia coli fumarate reductase decoupled from electron transport. Proc Natl Acad Sci U S A. 1986;83:2056-60 pubmed
    ..of four nonidentical subunits organized into two domains: FrdA and -B (a membrane-extrinsic catalytic domain) and FrdC and -D (a transmembrane anchor domain)...
  19. Jones H, Gunsalus R. Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate. J Bacteriol. 1985;164:1100-9 pubmed
  20. Westenberg D, Gunsalus R, Ackrell B, Cecchini G. Electron transfer from menaquinol to fumarate. Fumarate reductase anchor polypeptide mutants of Escherichia coli. J Biol Chem. 1990;265:19560-7 pubmed
    ..domain, FrdA and FrdB, are anchored to the cytoplasmic membrane surface by two small hydrophobic polypeptides, FrdC and FrdD, which are also required for the enzyme to interact with quinone...
  21. Iverson T, Luna Chavez C, Cecchini G, Rees D. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 1999;284:1961-6 pubmed
    ..Although fumarate reductase is not associated with any proton-pumping function, the two quinones are positioned on opposite sides of the membrane in an arrangement similar to that of the Q-cycle organization observed for cytochrome bc1...
  22. Cecchini G, Ackrell B, Deshler J, Gunsalus R. Reconstitution of quinone reduction and characterization of Escherichia coli fumarate reductase activity. J Biol Chem. 1986;261:1808-14 pubmed
  23. Seaver L, Imlay J. Are respiratory enzymes the primary sources of intracellular hydrogen peroxide?. J Biol Chem. 2004;279:48742-50 pubmed
    ..That source has not yet been identified. In respiring cells the rate of H2O2 production was approximately 0.5% the rate of total oxygen consumption, with only modest changes when cells used different carbon sources. ..
  24. Latour D, Weiner J. Assembly of Escherichia coli fumarate reductase holoenzyme. Biochem Cell Biol. 1989;67:251-9 pubmed
    ..b>FrdC and FrdD, the membrane anchor polypeptides, assembled rapidly into the membrane and then were capped with FrdA and ..
  25. Maklashina E, Iverson T, Sher Y, Kotlyar V, Andréll J, Mirza O, et al. Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. J Biol Chem. 2006;281:11357-65 pubmed
  26. Ackrell B, Cochran B, Cecchini G. Interactions of oxaloacetate with Escherichia coli fumarate reductase. Arch Biochem Biophys. 1989;268:26-34 pubmed
    ..The reason for the difference is not known. The redox potential of the FAD/FADH2 couple in FRD (Em approximately -55 mV) was also slightly more positive than that in cardiac succinate dehydrogenase (-90 mV). ..